High-purity recombinant Escherichia coli BirA, with no tag. For research use only.
Future Fields
Recombinant E. coli BirA, Tag Free
Regular price
$294.45 USD
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$294.45 USD
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Product at a Glance
- Synonyms: Biotin protein ligase, Biotin-[acetyl-CoA-carboxylase] ligase, Biotin-[acetyl-CoA-carboxylase] synthetase.
- Uniprot: P06709
- MW: 35.9 kDa
- Purity: ≥ 90% by SDS PAGE quantitative densitometry.
- Enzyme Activity: 500 units/µg
- Expression Host: Drosophila melanogaster
- Lyophilized from: 50 mM Tris-HCl pH 7.5, 150 mM NaCl, 2 mM DTT.
- For reconstitution and storage refer to PDS.
- Shipped as a lyophilized product, stable at room temperature for travel.
Product Application
- In vitro biotinylation of proteins and peptides: BirA is used to enzymatically biotinylate specific lysine residues on proteins with a biotin-acceptor peptide (BAP) tag. The biotinylated protein can then bind with high affinity to streptavidin or avidin for various downstream applications.
Product Sustainability
Manufactured in Future Fields' Green-certified lab located in Edmonton, Canada.
Quality Assays
Purity
Analysis method: SDS-PAGE under reducing conditions.
Staining: SYPRO™ Ruby (Cat. # S12000).
Purity: 95% by quantitative densitometry.
Molecular weight: BirA migrates at 30.3 kDa.
Molecular weight marker: Precision Plus Protein™ Unstained Standard (Cat. # 1610363).
WB Functional Activity
Analysis method: SDS-PAGE under reducing conditions.
Western blot probe: Streptavidin (HRP-conjugated) (Cat. # STN-NH913).
Activity: Positive for biotinylation of MBP-A substrate. Enzyme activity confirmed at ≥ 500 Units/µg.
Molecular weight: Biotinylated MBP-A runs at 46.1 kDa.
Molecular weight marker: Precision Plus Protein™ Unstained Standard (Cat. # 1610363).
Additional Characterization
Identity verified by mass spectrometry and western blot. Results available on request.
Description
BirA, also known as biotin protein ligase (BPL), is a multifunctional monomeric enzyme that belongs to the group II biotin-protein ligase family. It is also referred to as biotin operon repressor, biotin-[acetyl-CoA-carboxylase] ligase, and biotin-[acetyl-CoA-carboxylase] synthetase. In Escherichia coli, BirA serves dual roles: as a DNA-binding protein that represses the biotin biosynthesis operon and as an enzyme catalyzing the ATP-dependent biotinylation of specific lysine residues on biotin-accepting proteins or peptides, such as carboxyl carrier protein (BCCP) and AviTag fusion proteins.
Structurally, BirA comprises an N-terminal helix-turn-helix DNA-binding domain, a catalytic core responsible for synthesizing biotinyl 5'-adenylate (bio-5'-AMP), and a C-terminal domain that contributes to DNA binding, dimerization, and catalytic activity. The enzyme's GRGRRG motif near the biotin-binding site facilitates ATP binding, and its dynamic active-site loop undergoes structural ordering upon biotin binding.
BirA-mediated precise biotinylation enables the use of (strept)avidin-biotin interactions in diverse biochemical and cell biology applications, including protein capture, immobilization, multimerization, and molecular bridging. With its exceptional specificity, BirA biotinylates only one out of over 4,000 proteins in E. coli, ensuring targeted modification critical for research and industrial processes. This versatility makes it a powerful tool in protein engineering, affinity studies, and diagnostic development.
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